title: Characterization of hydrophobicity gradients prepared by means of radio frequency plasma discharge.
abstract: A hydrophobicity gradient was created by gradually exposing a polydimethylsiloxane film to a radio frequency glow discharge in an oxygen atmosphere. A change in contact angle from 100 to 0 degrees was measured along the gradient surface by means of the Wilhelmy balance technique. The gradient surface was characterized by studying the adsorption from single protein solutions of human albumin, IgG and fibrinogen using total internal reflectance fluorescence (TIRF). Generally, adsorption values similar to monolayer capacities were measured on the hydrophobic side. The adsorption decreased towards the hydrophilic end in correspondence with the change in contact angle. The displacement of proteins with a ethylene oxide-propylene oxide copolymer (EO70PO100EO70) was higher on the hydrophobic side than on the hydrophilic side. Albumin showed an adsorption peak in the wetting transition region, indicating a very strong affinity.
authors.affiliation: Center for Biopolymers at Interface, University of Utah, Salt Lake City, 84112.
authors.forename: C G
authors.initials: CG
authors.lastname: Gölander
authors.forename: W G
authors.initials: WG
authors.lastname: Pitt
mesh_terms: D000327:Adsorption; D000418:Albumins; D001672:Biocompatible Materials; D004129:Dimethylpolysiloxanes; D005240:Feasibility Studies; D005340:Fibrinogen; D006801:Humans; D007074:Immunoglobulin G; D008954:Models, Biological; D010100:Oxygen; D011506:Proteins; D011846:Radio Waves; D012828:Silicones; D013499:Surface Properties
chemical_list: D000418:Albumins; D001672:Biocompatible Materials; D004129:Dimethylpolysiloxanes; D007074:Immunoglobulin G; D011506:Proteins; D012828:Silicones; C013830:baysilon; D005340:Fibrinogen; D010100:Oxygen